ID PRP28_SCLS1 Reviewed; 816 AA.
AC A7EGG4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp28;
DE EC=3.6.4.13;
GN Name=prp28; ORFNames=SS1G_04405;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA splicing. May
CC destabilize the U1/5' splice site duplex to permit an effective
CC competition for the 5' splice site by the U6 snRNA, resulting in the
CC switch between U1 and U6 at the 5' splice site. May also act to unwind
CC the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating
CC the first covalent step of splicing (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: Component of the U5 snRNP complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC subfamily. {ECO:0000305}.
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DR EMBL; CH476625; EDO01930.1; -; Genomic_DNA.
DR RefSeq; XP_001594598.1; XM_001594548.1.
DR AlphaFoldDB; A7EGG4; -.
DR SMR; A7EGG4; -.
DR STRING; 665079.A7EGG4; -.
DR EnsemblFungi; EDO01930; EDO01930; SS1G_04405.
DR GeneID; 5491199; -.
DR KEGG; ssl:SS1G_04405; -.
DR eggNOG; KOG0333; Eukaryota.
DR HOGENOM; CLU_003041_11_3_1; -.
DR InParanoid; A7EGG4; -.
DR OMA; ARDIKHM; -.
DR OrthoDB; 5487240at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd17945; DEADc_DDX23; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..816
FT /note="Pre-mRNA-splicing ATP-dependent RNA helicase prp28"
FT /id="PRO_0000310208"
FT DOMAIN 410..613
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 624..787
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 379..407
FT /note="Q motif"
FT MOTIF 536..539
FT /note="DEAD box"
FT COMPBIAS 18..65
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 423..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 816 AA; 89525 MW; 8507DCE267C58C15 CRC64;
MASNGYLNSI DAVPPPLIDS DGRPPSPPPP PPDSFVPPPP PSSLAPPPPP SSDLPPPPPS
ELQPPPPEPK KKKGWGAPKP GPLSIEDILK KKKEADEAAA KPKFLSKAAR EKLALEKRAK
EVEEQRRKRE SEQDNRIPVG TVNGNGYGAA NGRDGYERSH QQDNARRDSS FVPTGPRAMR
NGQQNRPSSD KPNDMEPPPK SAKPATTAAG SSKASVAGEK RPANAEDLQA ALIRTRYMGA
ETNQSTFSAK KKRRRTTEKK FNFEWNAEED TSPDYNPIYQ NRAEAGLYGR GRLAGFAEDE
AATLKYAKAL EERDIEAGSA RAREIVEMER RRKEDAGRNS LDKHWSEKKL EHMRERDWRI
FKEDFNISTK GGAIPNPMRS WSESKLPKRL LDVINQVGYD EPSAVQRAAI PIALQARDLI
GVAVTGSGKT AAFLLPLLVY ISELPPLNEF TKNDGPYAII LAPTRELAQQ IEVEAKKFAT
PLGFTCVSIV GGHSLEEQSY NLRNGAEIII ATPGRLVDCI ERRVLVLGQC CYIIMDEADR
MIDLGFEESV NKILDALPVS NEKPDTDDAE DAQAMSRHLG GKDRYRQTMM YTATMPPAVE
KIAKKYLRRP AIVTIGNIGE AVETVEQRVE FVAGEDKRKK RLNEILASGE FQPPIIVFVN
IKRNCDAVAR DIKHMGFTSV TLHGSKTQEQ REAALASVRS GATNVLVATD LAGRGIDVPD
VSLVVNFNMA TNIESYTHRI GRTGRAGKSG VAITFLGNED ADTMYDLKQM LMKSSISRVP
EELRKHEAAQ QKSQRGQGLK KIEEGGFGGK GGAGGC
//
